Diaminopimelate decarboxylase, LysA (IPR002986)

Short name: DAP_deCOOHase_LysA

Overlapping homologous superfamilies

Family relationships


Pyridoxal-dependent decarboxylases that act on ornithine-, lysine-, arginine- and related substrates can be classified into different families on the basis of sequence similarity [PMID: 3143046, PMID: 8181483]. One of these families includes ornithine decarboxylase (ODC), which catalyses the transformation of ornithine into putrescine; prokaryotic diaminopimelate decarboxylase, which catalyses the conversion of diaminopimelate into lysine; Pseudomonas syringae pv. tabaci protein, tabA, which is probably involved in tabtoxin biosynthesis and is similar to diaminopimelate decarboxylase; and bacterial and plant biosynthetic arginine decarboxylase, which catalyses the transformation of arginine into agmatine, the first step in putrescine synthesis from arginine.

Although these proteins, which are known collectively as group IV decarboxylases [PMID: 8181483], probably share a common evolutionary origin, their levels of sequence similarity are low, being confined to a few short conserved regions. These conserved motifs suggest a common structural arrangement for positioning of substrate and the cofactor pyridoxal 5'-phosphate among bacterial diaminopimelate ddecarboxylases, eukaryotic ornithine decarboxylases and arginine decarboxylases [PMID: 8215365].

This entry represents the diaminopimelate decarboxylase LysA, which converts meso-diaminopimelate into lysine and is the last step of the DAP lysine biosynthetic pathway. The structure of bacterial diaminopimelate decarboxylase has been determined [PMID: 12637582].

GO terms

Biological Process

GO:0009089 lysine biosynthetic process via diaminopimelate

Molecular Function

GO:0008836 diaminopimelate decarboxylase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.